ID   SLB_GLOBL               Reviewed;         146 AA.
AC   Q9YI92;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Snaclec mamushigin subunit beta;
DE   Flags: Precursor;
OS   Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-56, SUBUNIT, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:9657448}, and Venom gland;
RX   PubMed=9657448;
RA   Sakurai Y., Fujimura Y., Kokubo T., Imamura K., Kawasaki T., Handa M.,
RA   Suzuki M., Matsui T., Titani K., Yoshioka A.;
RT   "The cDNA cloning and molecular characterization of a snake venom platelet
RT   glycoprotein Ib-binding protein, mamushigin, from Agkistrodon halys
RT   blomhoffii venom.";
RL   Thromb. Haemost. 79:1199-1207(1998).
CC   -!- FUNCTION: Binds to platelet GPIbalpha (GP1BA) and enhances platelet
CC       aggregation at low-shear stress. At high-shear stress, blocks platelet
CC       aggregation in a dose-dependent manner.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:9657448}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=15413; Mass_error=6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9657448};
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AB019616; BAA34425.1; -; mRNA.
DR   AlphaFoldDB; Q9YI92; -.
DR   SMR; Q9YI92; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IDA:UniProtKB.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:9657448"
FT   CHAIN           24..146
FT                   /note="Snaclec mamushigin subunit beta"
FT                   /id="PRO_0000017527"
FT   DOMAIN          32..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain (with C-103 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   146 AA;  17064 MW;  9EDA84BDCC24E76D CRC64;
     MGRFIFLSFG LLVVFVSLSG TGADCPSDWS SYEGHCYRVF QKEMTWEDAE KFCTQQRKES
     HLVSFHSSEE VDFVVSMTWP ILKYDFVWIG LNNIWNECMV EWTDGTRLSH NAWITESECI
     AAKTTDNQWL SRPCSRTYNV VCKFQE